ID PDE6_DROER Reviewed; 1131 AA. AC B3P3K2; DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot. DT 02-SEP-2008, sequence version 1. DT 24-JAN-2024, entry version 72. DE RecName: Full=cGMP-specific 3',5'-cyclic phosphodiesterase {ECO:0000250|UniProtKB:Q9VFI9}; DE EC=3.1.4.35; DE Flags: Precursor; GN Name=Pde6 {ECO:0000250|UniProtKB:Q9VFI9}; ORFNames=GG21262; OS Drosophila erecta (Fruit fly). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea; OC Drosophilidae; Drosophila; Sophophora. OX NCBI_TaxID=7220; RN [1] {ECO:0000312|EMBL:EDV48890.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Tucson 14021-0224.01 {ECO:0000312|EMBL:EDV48890.1}; RX PubMed=17994087; DOI=10.1038/nature06341; RG Drosophila 12 genomes consortium; RT "Evolution of genes and genomes on the Drosophila phylogeny."; RL Nature 450:203-218(2007). CC -!- FUNCTION: Has a role regulating cGMP transport in Malpighian tubule CC principal cells. {ECO:0000250|UniProtKB:Q9VFI9}. CC -!- CATALYTIC ACTIVITY: CC Reaction=3',5'-cyclic GMP + H2O = GMP + H(+); Xref=Rhea:RHEA:16957, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57746, CC ChEBI:CHEBI:58115; EC=3.1.4.35; CC Evidence={ECO:0000250|UniProtKB:Q9VFI9}; CC -!- COFACTOR: CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; CC Evidence={ECO:0000250}; CC Note=Binds 2 divalent metal cations per subunit. Site 1 may CC preferentially bind zinc ions, while site 2 has a preference for CC magnesium and/or manganese ions. {ECO:0000250}; CC -!- SUBUNIT: Interacts with PrBP. {ECO:0000250|UniProtKB:Q9VFI9}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9VFI9}; CC Lipid-anchor {ECO:0000250|UniProtKB:Q9VFI9}; Cytoplasmic side CC {ECO:0000250|UniProtKB:Q9VFI9}. CC -!- SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase family. CC {ECO:0000255}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CH954181; EDV48890.1; -; Genomic_DNA. DR RefSeq; XP_001979932.2; XM_001979896.2. DR AlphaFoldDB; B3P3K2; -. DR SMR; B3P3K2; -. DR GeneID; 6552139; -. DR KEGG; der:6552139; -. DR eggNOG; KOG3689; Eukaryota. DR HOGENOM; CLU_006980_0_2_1; -. DR OMA; ATIRMFK; -. DR OrthoDB; 5479253at2759; -. DR PhylomeDB; B3P3K2; -. DR ChiTaRS; Pde6; fly. DR Proteomes; UP000008711; Unassembled WGS sequence. DR GO; GO:0016020; C:membrane; ISS:UniProtKB. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0047555; F:3',5'-cyclic-GMP phosphodiesterase activity; ISS:UniProtKB. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0046068; P:cGMP metabolic process; ISS:UniProtKB. DR GO; GO:0007165; P:signal transduction; IEA:InterPro. DR CDD; cd00077; HDc; 1. DR Gene3D; 3.30.450.40; -; 2. DR Gene3D; 1.10.1300.10; 3'5'-cyclic nucleotide phosphodiesterase, catalytic domain; 1. DR InterPro; IPR003018; GAF. DR InterPro; IPR029016; GAF-like_dom_sf. DR InterPro; IPR003607; HD/PDEase_dom. DR InterPro; IPR023088; PDEase. DR InterPro; IPR002073; PDEase_catalytic_dom. DR InterPro; IPR036971; PDEase_catalytic_dom_sf. DR InterPro; IPR023174; PDEase_CS. DR PANTHER; PTHR11347; CYCLIC NUCLEOTIDE PHOSPHODIESTERASE; 1. DR PANTHER; PTHR11347:SF216; PHOSPHODIESTERASE; 1. DR Pfam; PF01590; GAF; 2. DR Pfam; PF00233; PDEase_I; 1. DR PRINTS; PR00387; PDIESTERASE1. DR SMART; SM00065; GAF; 2. DR SMART; SM00471; HDc; 1. DR SUPFAM; SSF55781; GAF domain-like; 2. DR SUPFAM; SSF109604; HD-domain/PDEase-like; 1. DR PROSITE; PS00126; PDEASE_I_1; 1. DR PROSITE; PS51845; PDEASE_I_2; 1. PE 3: Inferred from homology; KW Cell membrane; cGMP; Hydrolase; Lipoprotein; Membrane; Metal-binding; KW Methylation; Prenylation; Repeat. FT CHAIN 1..1128 FT /note="cGMP-specific 3',5'-cyclic phosphodiesterase" FT /id="PRO_0000363686" FT PROPEP 1129..1131 FT /note="Removed in mature form" FT /evidence="ECO:0000250|UniProtKB:Q9VFI9" FT /id="PRO_0000363687" FT DOMAIN 255..412 FT /note="GAF 1" FT /evidence="ECO:0000255" FT DOMAIN 444..625 FT /note="GAF 2" FT /evidence="ECO:0000255" FT DOMAIN 655..978 FT /note="PDEase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01192" FT REGION 1..26 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 42..150 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1019..1048 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1078..1131 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 77..93 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 104..150 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1087..1118 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 731 FT /note="Proton donor" FT /evidence="ECO:0000250" FT BINDING 735 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 771 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 772 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 772 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 882 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="1" FT /evidence="ECO:0000250" FT MOD_RES 1128 FT /note="Cysteine methyl ester" FT /evidence="ECO:0000250|UniProtKB:Q9VFI9" FT LIPID 1128 FT /note="S-farnesyl cysteine" FT /evidence="ECO:0000250|UniProtKB:Q9VFI9" SQ SEQUENCE 1131 AA; 125578 MW; D63B518C430CAE35 CRC64; MTDVSSPAGG AASPVEMATS SSSAATTLTN GANKTAISTA AGVAPGAVPG PGSAAIPASS SSGNQVKLEH HHRQSNNNRP AATNRSSETK LRSPAGESDG ASRLMTPAGS SSTPSQSPSP SQSPSQASIQ TQTSQQDRLA KASTTASQQD VDEVARLFEE KPEAFEKWLT ERAPPEALSR LQEFIENRKP HKRPSVTSDL FQQWMAASPT VQQKSPRSLS NSSASSIPEC RRHLMDLDEG ELFMELIRDV ANELDIDVLC HKILVNVGLL THADRGSLFL AKGTPTNKYL VAKLFDVTQK TALKDAVTRA SAEEIIIPFG IGIAGMVAQT KQMINIKEAY KDARFNCEID LKTGYKTNAI LCMPICNYEG DIIGVAQIIN KTNGGCFKGC MEFDEHDVEI FRRYLTFCGI GIQNAQLFEM SVQEYRRNQI LLNLARSIFE EQNNLECLVT KIMTEARELL KCERCSVFLV DLDCCEASHL EKIIEKPNQP ATRAIKSADS FEEKKMRNRF TVLFELGGEY QAANVSRPSV SELSSSTLAQ IAQFVATTGQ TVNICDVIEW VRDHNQIRAE DEIDSTQAIL CMPIMNAQKK VIGVAQLINK ANGVPFTDSD ASIFEAFAIF CGLGIHNTQM YENACKLMAK QKVALECLSY HATASQDQTE KLTQDVIAEA ESYNLYSFTF TDFELVDDDT CRAVLRMFMQ CNLVSQFQIP YDVLCRWVLS VRKNYRPVKY HNWRHALNVA QTMFAMLKTG KMERFMTDLE ILGLLVACLC HDLDHRGTNN AFQTKTESPL AILYTTSTME HHHFDQCVMI LNSEGNNIFQ ALSPEDYRSV MKTVESAILS TDLAMYFKKR NAFLELVENG EFDWQGEEKK DLLCGMMMTA CDVSAIAKPW EVQHKVAKLV ADEFFDQGDL EKLQLNTQPV AMMDRERKDE LPKMQVGFID VICLPLYRVL CDTFPWITPL YEGTLENRRN WQDLAEKVEM GLTWIDHDTI DKPVEEFAAC ADEEIKDIEF TVTTLNCNQQ SQHGSEDSHT PEHQRSGSRL SMKKTGALGK AVRSKLSKTL YNSMDGSKPK TSLKLLESHV SEDMDDKSPT SPSQPQASGS MGRMSASSST SSAGGQMVDK SKKRSKLCAL L //